CHARACTERIZATION OF SOLUBILIZED CYTOCHROME P‐450

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Abstract
Porcine liver microsomes were subjected to digitonin, n‐butanol and sonication treatment to solubilize cytochrome P‐450 and other mixed‐function oxidation components. The best preparation achieved with 2% digitonin gave characteristic P‐450, CN‐and NO2‐ difference spectra. It was further purified by ammonium sulfate fractionation and column chromatography. Column chromatography resulted in the separation of cytochrome P‐450 subparticles from cytochrome P‐420 subparticles; both contained negligible quantities of cytochrome b5 and significant amounts of ferricyanide reductase and NADPH oxidase activity.